ID A0A2K6RJB5_RHIRO Unreviewed; 1192 AA.
AC A0A2K6RJB5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 19 {ECO:0000313|Ensembl:ENSRROP00000041128.1};
GN Name=ADAMTS19 {ECO:0000313|Ensembl:ENSRROP00000041128.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000041128.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000041128.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR AlphaFoldDB; A0A2K6RJB5; -.
DR Ensembl; ENSRROT00000065623.1; ENSRROP00000041128.1; ENSRROG00000043770.1.
DR GeneTree; ENSGT00940000161018; -.
DR OMA; QHAEPDG; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF197; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 19; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 310..530
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1145..1184
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 32..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 468
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 477
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 525
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 386..451
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 426..433
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 445..525
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 484..509
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 554..578
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 565..586
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 573..605
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 599..610
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 630..665
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 634..670
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 645..655
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1192 AA; 132048 MW; 00BD53E7883386CD CRC64;
QTHLDPTLLS LQFAPDREEW EVVFPALWRR EPVDTAGGSG GSADPGWVRG VGGGGSARAQ
AAGSSREVRS VAPVPLEEPV EGRSESRLRP PPPSEGEEDE ELESQELPRG SSGAAALSPG
APASWQPPPP PQPPPSPPPA HHAAPDGDEV LLRIPAFSRD LYLLLRRDGR FLAPRFAVEQ
RPNPGPGPTG AASAPQPPAP PDAGCFYTGA VLRHPGSLAS FSTCGGGLMG FIQLNEDFIF
IEPLNDTMAI TGHPHRVYRQ KRSMEEKVTE KSALHSHYCG IISDKGRPRS RKIAESGRGK
RYSYKLPQEY NIETVVVADP AMVSYHGADA ARRFILTILN MVFNLFQHKS LGVQVNLRVI
KLILLHETPP DLYIGHHGEK MLESFCKWQH EEFGKKNDIH LEMSTSWGED MNSVDAAILI
TRKDFCVHKD EPCDTVGIAY LSGMCSEKRK CIIAEDNGLN LAFTIAHEMG HNMGINHDND
HPSCADGLHI MSGEWIKGQN LGDVSWSRCS KEDLERFLRS KASNCLLQTN PQSVNSVMVP
SKLPGMTYTA DEQCQILFGP LASFCQEMQH VICTGLWCKV GGEKECKTKL DPPMDGTDCD
PGKWCKAGEC TSRTSAPEHL AGEWSLWSPC SRTCSAGISS RERKCPGLGS EARDCNGPRK
QYRICENPPC PAGLPGFRDW QCQAYSVRTS SPKHVLQWQA VLDEEKPCAL FCSPVGKEQP
ILLSEKVMDG TSCGYQGLDI CANGRCQKVG CDGLLGSLAR EDHCGVCNGN GKSCKIIKGD
FNHTRGAGYV EVLVIPAGAR RIKVVEEKPA HSYLALRDAG KQSINSDWKI EHSGAFNLAG
TTVHYVRRGL WEKISAKGPT TAPLHLLVLL FQDQNYGLHY EYTIPSDPLP ENQSSKAPEP
LFMWTHTSWE DCDATCGGGE RKTTVSCTKI MSKNISIVDN KKCKYLTKPE PQIRKCNEQP
CQTRWMMTEW TPCSRTCGKG MQSRQVACTQ QLSNGTLIRA RERDCIGPKP ASAQRCEGQD
CMTVWEAGVW SECSVKCGKG VRHRTVRCTN PRKKCVLSTR PREAEDCEDY SKCYVWRMGD
WSKCSITCGK GMQSRVIQCM HKITGRHGNE CFSSEKPAAY RPCHLQPCNE KINVNTITSP
RLAALTFKCL GDQWPVYCRV IREKNLCQDM RWYQRCCETC RDFYAQKLQQ KS
//
